2vl9

X-ray diffraction
2.7Å resolution

Oxidized form of human peroxiredoxin 5

Released:

Function and Biology Details

Reaction catalysed:
2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peroxiredoxin-5, mitochondrial Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 173 amino acids
Theoretical weight: 18.31 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli M15
UniProt:
  • Canonical: P30044 (Residues: 54-214; Coverage: 75%)
Gene names: ACR1, PRDX5, SBBI10
Sequence domains: Redoxin
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: P3121
Unit cell:
a: 75.87Å b: 75.87Å c: 193.254Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.186 0.184 0.239
Expression system: Escherichia coli M15